Abstract
BackgroundOsteoglycin (OGN, a.k.a. mimecan) belongs to cluster III of the small leucine-rich proteoglycans (SLRP) of the extracellular matrix (ECM). In vertebrates OGN is a characteristic ECM protein of bone. In the present study we explore the evolution of SLRP III and OGN in teleosts that have a skeleton adapted to an aquatic environment.ResultsThe SLRP gene family has been conserved since the separation of chondrichthyes and osteichthyes. Few gene duplicates of the SLRP III family exist even in the teleosts that experienced a specific whole genome duplication. One exception is ogn for which duplicate copies were identified in fish genomes. The ogn promoter sequence and in vitro mesenchymal stem cell (MSC) cultures suggest the duplicate ogn genes acquired divergent functions. In gilthead sea bream (Sparus aurata) ogn1 was up-regulated during osteoblast and myocyte differentiation in vitro, while ogn2 was severely down-regulated during bone-derived MSCs differentiation into adipocytes in vitro.ConclusionsOverall, the phylogenetic analysis indicates that the SLRP III family in vertebrates has been under conservative evolutionary pressure. The retention of the ogn gene duplicates in teleosts was linked with the acquisition of different functions. The acquisition by OGN of functions other than that of a bone ECM protein occurred early in the vertebrate lineage.
Highlights
Osteoglycin (OGN, a.k.a. mimecan) belongs to cluster III of the small leucine-rich proteoglycans (SLRP) of the extracellular matrix (ECM)
Ogn1 transcripts are up-regulated in the early stages of osteoblast and myocyte differentiation in vitro;
Ogn2 transcripts are down-regulated in bonederived Mesenchymal stem cells (MSCs) under osteoinductive and adipogenic conditions; Background The extracellular matrix (ECM) is important in multicellular organisms and establishes the basic
Summary
Osteoglycin (OGN, a.k.a. mimecan) belongs to cluster III of the small leucine-rich proteoglycans (SLRP) of the extracellular matrix (ECM). (SLRP) family comprises the largest class of proteoglycans in the ECM. They are extracellular proteins with a small protein core, harbouring tandem leucine-rich repeats (LRRs) that may contain one or more glycosaminoglycan side chains, there are some excep tions [9, 10]. The SLRP family is clustered into 5 main groups (cluster I-V) when protein and gene homology, chromosome localization and the presence and spacing of the classical N-terminal cysteine-rich repeats are considered [1, 11,12,13]. Functional compensation can occur between SLRPs and an example of this is the up-regulation of decorin when biglycan is lost in hu mans [14]
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